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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
1992-1-9
pubmed:databankReference
pubmed:abstractText
cDNA clones containing sequence similarity to the multifunctional vertebrate protein disulfide-isomerase (PDI, EC 5.3.4.1) were isolated from an alfalfa (Medicago sativa L.) cDNA library by screening with a cDNA sequence encoding human PDI. The polypeptide encoded by a clone designated B2 consisted of 512 amino acids and was characterized by a 24-amino acid hydrophobic leader sequence, two regions with absolute identity to the vertebrate PDI active site (Ala-Pro-Trp-Cys-Gly-His-Cys-Lys), and a C-terminal endoplasmic reticulum retention signal (Lys-Asp-Glu-Leu). The overall identity of the B2 sequence to that of human PDI was 35% at the amino acid level (79% when conservative substitutions were included) and 39% at the nucleotide level; this included homology between B2 and the region of human PDI believed to be involved in binding estrogens. The deduced amino acid sequence of B2 was also 35% identical to that of a rat form I phosphatidylinositol-specific phospholipase C. Lysates from Escherichia coli cells harboring an expression plasmid bearing the B2 sequence contained significantly elevated levels of PDI activity. Southern analysis indicated the presence of a small PDI-related gene family in alfalfa, of which B2 appeared to correspond to a single gene. An approximately 2-kilobase B2 transcript was expressed in all alfalfa organs tested. In alfalfa cell suspension cultures, B2 transcripts were strongly induced by tunicamycin but not by exposure to fungal elicitor.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-16667176, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-16667295, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-16667764, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-1840696, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2002068, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2025222, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2254345, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2295602, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2344363, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2351674, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2441623, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2458190, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2544299, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2558866, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2668279, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-271968, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-2851999, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3034602, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3036064, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3243435, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3387233, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3398923, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3545499, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3619939, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3627262, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3714490, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3840230, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-3907854, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-6312838, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-7174650, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-903355, http://linkedlifedata.com/resource/pubmed/commentcorrection/1720555-942051
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
88
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10941-5
pubmed:dateRevised
2010-9-7
pubmed:meshHeading
pubmed-meshheading:1720555-Humans, pubmed-meshheading:1720555-Animals, pubmed-meshheading:1720555-Vertebrates, pubmed-meshheading:1720555-Medicago sativa, pubmed-meshheading:1720555-DNA, pubmed-meshheading:1720555-Escherichia coli, pubmed-meshheading:1720555-RNA, pubmed-meshheading:1720555-Plant Proteins, pubmed-meshheading:1720555-Isomerases, pubmed-meshheading:1720555-Membrane Proteins, pubmed-meshheading:1720555-Cells, Cultured, pubmed-meshheading:1720555-Amino Acid Sequence, pubmed-meshheading:1720555-Macromolecular Substances, pubmed-meshheading:1720555-Binding Sites, pubmed-meshheading:1720555-Molecular Sequence Data, pubmed-meshheading:1720555-Transcription, Genetic, pubmed-meshheading:1720555-Phosphoric Diester Hydrolases, pubmed-meshheading:1720555-Cloning, Molecular, pubmed-meshheading:1720555-Oligodeoxyribonucleotides, pubmed-meshheading:1720555-Restriction Mapping, pubmed-meshheading:1720555-Sequence Homology, Nucleic Acid
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